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KMID : 0376219830200010175
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Chonnam Medical Journal
1983 Volume.20 No. 1 p.175 ~ p.182
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Peroxidation of Membrane Lipids and Proteins in Human Erythrocytes
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李民化/Lee, Min-wha
安鳳煥/梁誠烈/朴炳柱/任哲完/Ahn, Bong-whan/Yang, Sung-yeul/Park, Byung-ju/Ihm, Chull-wan
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Abstract
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Dihydroxyfumaric acid (DHF) and ascorbic acid (AA), in the presence of FeSO4, caused a lipid peroxidation in human erythrocyte membrane in vitro. Additionally, these agents caused a decrease in bands 1 and 2 components of spectra in the membrane proteins and an increase in high molecular weight protein polymers.
The membrane lipid peroxidation by DHF and AA was partially inhibited by catalase or peroxides, but not by superoxide dismutase, indicating that hydrogen peroxide rather than superoxide radical is involved in this process.
The DHF-and AA-induced changes in spectrin were also observed even when spectrin was purified free of lipid contaminants from erythrocyte membrane. When 1-mercaptoethanol was added to the purified spectrin, the spectrin denaturation by DHF and AA did not occur.
These results suggest that the DHF-and AA-induced denaturation of membrane spectrin need not involve membrane lipid peroxidation, and that the polymerization of spectrin may be caused by disulfide bond formation in the spectrin molecule.
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